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pMD18-T Simple Vector is a high-efficiency TA cloning vector constructed from pUC18, of which the initial multiple cloning sites (MCS) were destroyed. Thus the cDNA should be amplified by PCR with primers containing a restriction site for subclone. Competent cells appropriate for pUC18 are also appropriated for the Vector, e.g. JM109, DH5α, TOP10. The pMD18-T Simple Vector is 2.6kb in size. Selection of the plasmid in E. coli is conferred by the ampicillin resistance gene. The coding sequence was inserted by TA cloning at site 425.
The coding sequence can be amplified by PCR with M13-47 and RV-M primers.
|Human PVRL1 ORF mammalian expression plasmid, C-GFPSpark tag||HG11611-ACG|
|Human PVRL1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG11611-ACR|
|Human PVRL1 ORF mammalian expression plasmid, C-Flag tag||HG11611-CF|
|Human PVRL1 ORF mammalian expression plasmid, C-His tag||HG11611-CH|
|Human PVRL1 ORF mammalian expression plasmid, C-Myc tag||HG11611-CM|
|Human PVRL1 ORF mammalian expression plasmid, C-HA tag||HG11611-CY|
|Human PVRL1 ORF mammalian expression plasmid, N-Flag tag||HG11611-NF|
|Human PVRL1 ORF mammalian expression plasmid, N-His tag||HG11611-NH|
|Human PVRL1 ORF mammalian expression plasmid, N-Myc tag||HG11611-NM|
|Human PVRL1 ORF mammalian expression plasmid, N-HA tag||HG11611-NY|
|Human PVRL1 natural ORF mammalian expression plasmid||HG11611-UT|
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Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin-1; CD111), also known as PVRL1 is a cell adhesion molecule belonging to the immunoglobulin superfamily that can bind to virion glycoprotein D (gD) to mediate entry of herpes simplex viruses (HSV) and pseudorabies virus (PRV). CD111/Nectin-1/PVRL1 colocalizes with E-cadherin at adherens junctions in epithelial cells. The disruption of cell junctions can result in the redistribution of nectin-1. To determine whether disruption of junctions by calcium depletion influenced the susceptibility of epithelial cells to viral entry, Madin-Darby canine kidney cells expressing endogenous nectin-1 or transfected human nectin-1 were tested for the ability to bind soluble forms of viral gD and to be infected by HSV and PRV, before and after calcium depletion. It has been revealed that binding of HSV and PRV gD was localized to adherens junctions in cells maintained in normal medium but was distributed, along with nectin-1, over the entire cell surface after calcium depletion. Both the binding of gD and the fraction of cells that could be infected by HSV-1 and PRV were enhanced by calcium depletion. Taken together, CD111/Nectin-1/PVRL1 confined to adherens junctions in epithelial cells is not very accessible to virus, whereas dissociation of cell junctions releases nectin-1 to serve more efficiently as an entry recptor.